MDGA2_RAT
ID MDGA2_RAT Reviewed; 949 AA.
AC P60756;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=MAM domain-containing glycosylphosphatidylinositol anchor protein 2;
DE AltName: Full=MAM domain-containing protein 1;
DE Flags: Precursor;
GN Name=Mdga2; Synonyms=Mamdc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Pons;
RX PubMed=15019943; DOI=10.1016/j.mcn.2003.10.016;
RA Litwack E.D., Babey R., Buser R., Gesemann M., O'Leary D.D.M.;
RT "Identification and characterization of two novel brain-derived
RT immunoglobulin superfamily members with a unique structural organization.";
RL Mol. Cell. Neurosci. 25:263-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.Q., Wu S.L., Liu S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=23248271; DOI=10.1073/pnas.1219987110;
RA Lee K., Kim Y., Lee S.-J., Qiang Y., Lee D., Lee H.W., Kim H., Je H.S.,
RA Suedhof T.C., Ko J.;
RT "MDGAs interact selectively with neuroligin-2 but not other neuroligins to
RT regulate inhibitory synapse development.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:336-341(2013).
CC -!- FUNCTION: May be involved in cell-cell interactions. {ECO:0000250}.
CC -!- SUBUNIT: Interacts (through the Ig-like domains) with NLGN2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in neuronal tissue.
CC Expressed in brain. {ECO:0000269|PubMed:15019943,
CC ECO:0000269|PubMed:23248271}.
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DR EMBL; AY371924; AAQ75750.1; -; mRNA.
DR RefSeq; NP_954890.1; NM_199269.1.
DR AlphaFoldDB; P60756; -.
DR SMR; P60756; -.
DR STRING; 10116.ENSRNOP00000000767; -.
DR GlyGen; P60756; 8 sites.
DR PaxDb; P60756; -.
DR PRIDE; P60756; -.
DR Ensembl; ENSRNOT00000000767; ENSRNOP00000000767; ENSRNOG00000000618.
DR GeneID; 314180; -.
DR KEGG; rno:314180; -.
DR UCSC; RGD:735131; rat.
DR CTD; 161357; -.
DR RGD; 735131; Mdga2.
DR eggNOG; ENOG502QSMD; Eukaryota.
DR GeneTree; ENSGT00940000155369; -.
DR HOGENOM; CLU_014908_0_0_1; -.
DR InParanoid; P60756; -.
DR OrthoDB; 118847at2759; -.
DR PhylomeDB; P60756; -.
DR TreeFam; TF330345; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:P60756; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Genevisible; P60756; RN.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0007389; P:pattern specification process; ISO:RGD.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:RGD.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; ISO:RGD.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IEP:HGNC-UCL.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000998; MAM_dom.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS50060; MAM_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..924
FT /note="MAM domain-containing glycosylphosphatidylinositol
FT anchor protein 2"
FT /id="PRO_0000014861"
FT PROPEP 925..949
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000292045"
FT DOMAIN 27..127
FT /note="Ig-like 1"
FT DOMAIN 134..232
FT /note="Ig-like 2"
FT DOMAIN 242..328
FT /note="Ig-like 3"
FT DOMAIN 340..436
FT /note="Ig-like 4"
FT DOMAIN 442..533
FT /note="Ig-like 5"
FT DOMAIN 540..627
FT /note="Ig-like 6"
FT DOMAIN 638..738
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 739..914
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT LIPID 924
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 159..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 264..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 359..417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 465..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 561..611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 949 AA; 106719 MW; BC955C0C6C1BB2B6 CRC64;
MDLVYGLVWL LTVLLEGISG QGVYAPPTVR IVHSGLACNI EEERYSERVY TIREGETLEL
TCLVTGHPRP QIRWTKTAGS ASDRFQDSSV FNETLRITSI QRHQGGRYYC KAENGLGSPA
IKSIRVDVYY LDDPVVTVHQ SIGEAKEQFY YERTVFLRCV ANSNPPVRYS WRRGQEVLLQ
GSDKGVEIYE PFFTQGETKI LKLKNLRPQD YANYSCIASV RNVCNIPDKM VSFRLSNKTA
SPSIKLLVDD PIVVNPGEAI TLVCVTTGGE PMPSLTWVRS FGTLPEKIVL NGGTLTIPAI
TSDDAGTYSC IANNNVGNPA KKSTNIIVRA LKKGRFWITP DPYHKDDNIQ IGREVKISCQ
VEAVPSEELT FSWFKNGRPL RSSERMVITQ TDPDVSPGTT NLDIIDLKFT DFGTYTCVAS
LKGGGISDIS IDVNISSSTV PPNLTVPQEK SPLVTREGDT IELQCQVTGK PKPIILWSRA
DKEVAMPDGT MQMESYDGTL RIVNVSREMS GMYRCQTSQY NGFNVKPREA LVQLIVQYPP
AVEPAFLEIR QGQDRSVTMS CRVLRAYPIR VLTYEWRLGN KLLRTGQFDS QEYTEYPLKS
LSNENYGVYN CSIINEAGAG RCSFLVTGKA YAPEFYYDTY NPVWQNRHRV YSYSLQWTQM
NPDAVDRIVA YRLGIRQAGQ QRWWEQEIKI NGNIQKGELI TYNLTELIKP EAYEVRLTPL
TKFGEGDSTI RVIKYTGEFH CGFEDGNICL FTQDDTDNFD WTKQSTATRN TKYTPNTGPN
ADRSGSKEGF YMYIETSRPR LEGEKARLLS PVFSIAPKNP YGPTNSAYCF SFFYHMYGQH
IGVLNVYLRL KGQTTIENPL WSSSGNKGQR WNEAHVNIYP ITSFQLIFEG IRGPGIEGDI
AIDDVSIAEG ECAKQDLPTK NSVDGAVGIL VHIWLFPVII LISILSPRR
